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Titolo:
Imbalance of antioxidant defense in mice lacking cellular prion protein
Autore:
Klamt, F; Dal-Pizzol, F; da Frota, MLC; Walz, R; Andrades, ME; da Silva, EG; Brentani, RR; Izquierdo, I; Moreira, JCF;
Indirizzi:
Univ Fed Rio Grande Sul, ICBS, Dept Bioquim, Lab Estresse Oxidat, BR-90035003 Porto Alegre, RS, Brazil Univ Fed Rio Grande Sul Porto Alegre RS Brazil BR-90035003 BC, RS, Brazil Univ Extremo Sul Catarinense, Dept Med, Criciuma, Brazil Univ Extremo Sul Catarinense Criciuma Brazil Dept Med, Criciuma, Brazil Univ Sao Paulo, Hosp Clin, Ctr Cirurgia Epilepsia, BR-14049 Ribeirao Preto, Brazil Univ Sao Paulo Ribeirao Preto Brazil BR-14049 049 Ribeirao Preto, Brazil Ludwig Inst Canc Res, Sao Paulo, Brazil Ludwig Inst Canc Res Sao Paulo Brazil Inst Canc Res, Sao Paulo, Brazil Univ Fed Rio Grande Sul, ICBS, Dept Bioquim, Ctr Memoria, Porto Alegre, RS, Brazil Univ Fed Rio Grande Sul Porto Alegre RS Brazil Porto Alegre, RS, Brazil
Titolo Testata:
FREE RADICAL BIOLOGY AND MEDICINE
fascicolo: 10, volume: 30, anno: 2001,
pagine: 1137 - 1144
SICI:
0891-5849(20010515)30:10<1137:IOADIM>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
ORNITHINE DECARBOXYLASE ACTIVITY; CREUTZFELDT-JAKOB-DISEASE; RAT-BRAIN SLICES; MOLECULAR-BIOLOGY; INDUCED ELEVATION; OXIDATIVE STRESS; CELLS; EXPRESSION; RADICALS; VARIANT;
Keywords:
prion diseases; PrPC; free radicals; superoxide dismutase; catalase; protein oxidation; lipid peroxidation; ornithine decarboxylase; oxidative stress;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Moreira, JCF Univ Fed Rio Grande Sul, ICBS, Dept Bioquim, Lab Estresse Oxidat, Rua Ramiro Barcelos 2600 Anexo, BR-90035003 Porto Alegre, RS, Brazil Univ Fed Rio Grande Sul Rua Ramiro Barcelos 2600 Anexo Porto Alegre RS Brazil BR-90035003 BC
Citazione:
F. Klamt et al., "Imbalance of antioxidant defense in mice lacking cellular prion protein", FREE RAD B, 30(10), 2001, pp. 1137-1144

Abstract

Prion diseases are fatal neurodegenerative disorders resulting from conformational changes in the prion protein from its normal cellular isoform, PrPC, to the infectious scrapie isoform, PrPSc. In spite of many studies, the physiological function of PrPC remains unknown. Recent work shows that PrPCbinds Cu2+. internalizing it into the cytoplasm. Since many antioxidant enzymes depend on Cu2+ (e.g., Cu/ZnSOD), their function could be affected in prion diseases. Here we investigate a possible relationship between PrPC and the cellular antioxidant systems in different structures isolated from PrPC knockout and wild-type mice by determining oxidative damage in protein and lipids and activity of antioxidant enzymes (CAT, SOD) and stress-adaptive enzymes (ODC). Our results show that. in the absence of PrPC, there is anincreased oxidation of lipid and protein in all structures investigated. Decreased SOD activity and changes in CAT/ODC activities were also observed. Taking into account these results, we suggest that the physiological function of PrPC is related to cellular antioxidant defenses. Therefore, during development of prion diseases, the whole organism becomes more sensitive toROS injury, leading to a progressive oxidative disruption of tissues and vital organs, especially the central nervous system. (C) 2001 Elsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 05:02:46